Use my Search Websuite to scan PubMed, PMCentral, Journal Hosts and Journal Archives, FullText. Kick-your-searchterm to multiple Engines kick-your-query now !>

A dictionary by aggregated review articles of nephrology, medicine and the life sciences Your one-stop-run pathway from word to the immediate pdf of peer-reviewed on-topic knowledge.

10.1074/jbc.M117.789263 http://scihub22266oqcxt.onion/10.1074/jbc.M117.789263 C5519374!5519374!28515318     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Biol+Chem 2017 ; 292 (29): 12256-66 Nephropedia Template TP {{tp|p=28515318|t=2017. Molecular mechanism of activation of class IA phosphoinositide 3-kinases (PI3Ks) by membrane-localized HRas |pdf=|usr=}}{{28515318}} gab.com Text Molecular mechanism of activation of class IA phosphoinositide 3-kinases (PI3Ks) by membrane-localized HRas JO: J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=28515318 #FOAvip Class IA PI3Ks are involved in the generation of the key lipid signaling molecule phosphatidylinositol 3,4,5-trisphosphate (PIP3), and inappropriate activation of this pathway is implicated in a multitude of human diseases, including cancer, inflammation, and primary immunodeficiencies. Class IA PI3Ks are activated downstream of the Ras superfamily of GTPases, and Ras?PI3K interaction plays a key role in promoting tumor formation and maintenance in Ras-driven tumors. Investigating the detailed molecular events in the Ras?PI3K interaction has been challenging because it occurs on a membrane surface. Here, using maleimide-functionalized lipid vesicles, we successfully generated membrane-resident HRas and evaluated its effect on PI3K signaling in lipid kinase assays and through analysis with hydrogen?deuterium exchange MS. We screened all class IA PI3K isoforms and found that HRas activates both p110? and p110? isoforms but does not activate p110?. The p110? and p110? activation by Ras was synergistic with activation by a soluble phosphopeptide derived from receptor tyrosine kinases. Hydrogen?deuterium exchange MS revealed that membrane-resident HRas, but not soluble HRas, enhances conformational changes associated with membrane binding by increasing membrane recruitment of both p110? and p110?. Together, these results afford detailed molecular insight into the Ras?PI3K signaling complex, provide a framework for screening Ras inhibitors, and shed light on the isoform specificity of Ras?PI3K interactions in a native membrane context. Twit Text FOAVip Molecular mechanism of activation of class IA phosphoinositide 3-kinases (PI3Ks) by membrane-localized HRas ????J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=28515318 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28515318 #FOAvip English Wikipedia <ref>{{Cite pmid|28515318}}</ref> Molecular mechanism of activation of class IA phosphoinositide 3-kinases (PI3Ks) by membrane-localized HRas #MMPMID28515318 Siempelkamp BD; Rathinaswamy MK; Jenkins ML; Burke JE J Biol Chem 2017[Jul]; 292 (29): 12256-66 PMID28515318show ga Class IA PI3Ks are involved in the generation of the key lipid signaling molecule phosphatidylinositol 3,4,5-trisphosphate (PIP3), and inappropriate activation of this pathway is implicated in a multitude of human diseases, including cancer, inflammation, and primary immunodeficiencies. Class IA PI3Ks are activated downstream of the Ras superfamily of GTPases, and Ras?PI3K interaction plays a key role in promoting tumor formation and maintenance in Ras-driven tumors. Investigating the detailed molecular events in the Ras?PI3K interaction has been challenging because it occurs on a membrane surface. Here, using maleimide-functionalized lipid vesicles, we successfully generated membrane-resident HRas and evaluated its effect on PI3K signaling in lipid kinase assays and through analysis with hydrogen?deuterium exchange MS. We screened all class IA PI3K isoforms and found that HRas activates both p110? and p110? isoforms but does not activate p110?. The p110? and p110? activation by Ras was synergistic with activation by a soluble phosphopeptide derived from receptor tyrosine kinases. Hydrogen?deuterium exchange MS revealed that membrane-resident HRas, but not soluble HRas, enhances conformational changes associated with membrane binding by increasing membrane recruitment of both p110? and p110?. Together, these results afford detailed molecular insight into the Ras?PI3K signaling complex, provide a framework for screening Ras inhibitors, and shed light on the isoform specificity of Ras?PI3K interactions in a native membrane context. äMolecular mechanism of activation of class IA phosphoinositide 3-kinas(epmc).pdf DeepDyve Pubget Overpricing